ID EPCAM_HUMAN Reviewed; 314 AA. AC P16422; P18180; Q6FG26; Q6FG49; Q96C47; Q9UCD0; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 2. DT 27-MAR-2024, entry version 215. DE RecName: Full=Epithelial cell adhesion molecule; DE Short=Ep-CAM; DE AltName: Full=Adenocarcinoma-associated antigen; DE AltName: Full=Cell surface glycoprotein Trop-1; DE AltName: Full=Epithelial cell surface antigen; DE AltName: Full=Epithelial glycoprotein; DE Short=EGP; DE AltName: Full=Epithelial glycoprotein 314; DE Short=EGP314; DE Short=hEGP314; DE AltName: Full=KS 1/4 antigen; DE AltName: Full=KSA; DE AltName: Full=Major gastrointestinal tumor-associated protein GA733-2; DE AltName: Full=Tumor-associated calcium signal transducer 1; DE AltName: CD_antigen=CD326; DE Flags: Precursor; GN Name=EPCAM; Synonyms=GA733-2, M1S2, M4S1, MIC18, TACSTD1, TROP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-115. RC TISSUE=Lung adenocarcinoma; RX PubMed=2463074; RA Strnad J., Hamilton A.E., Beavers L.S., Gamboa G.C., Apelgren L.D., RA Taber L.D., Sportsman J.R., Bumol T.F., Sharp J.D., Gadski R.A.; RT "Molecular cloning and characterization of a human RT adenocarcinoma/epithelial cell surface antigen complementary DNA."; RL Cancer Res. 49:314-317(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-115. RX PubMed=2469722; RA Perez M.S., Walker L.E.; RT "Isolation and characterization of a cDNA encoding the KS1/4 epithelial RT carcinoma marker."; RL J. Immunol. 142:3662-3667(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-115. RX PubMed=2108441; DOI=10.1073/pnas.87.7.2755; RA Simon B., Podolsky D.K., Moldenhauer G., Isselbacher K.J., RA Gattoni-Celli S., Brand S.J.; RT "Epithelial glycoprotein is a member of a family of epithelial cell surface RT antigens homologous to nidogen, a matrix adhesion protein."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2755-2759(1990). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Colon carcinoma; RX PubMed=2333300; DOI=10.1073/pnas.87.9.3542; RA Szala S., Froehlich M., Scollon M., Kasai Y., Steplewski Z., Koprowski H., RA Linnenbach A.J.; RT "Molecular cloning of cDNA for the carcinoma-associated antigen GA733-2."; RL Proc. Natl. Acad. Sci. U.S.A. 87:3542-3546(1990). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Lymphoma; RX PubMed=8382772; DOI=10.1128/mcb.13.3.1507-1515.1993; RA Linnenbach A.J., Seng B.A., Wu S., Robbins S., Scollon M., Pyrc J.J., RA Druck T., Huebner K.; RT "Retroposition in a family of carcinoma-associated antigen genes."; RL Mol. Cell. Biol. 13:1507-1515(1993). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-115. RC TISSUE=Ovary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-126. RC TISSUE=Placenta; RX PubMed=2911574; DOI=10.1073/pnas.86.1.27; RA Linnenbach A.J., Wojcierowski J., Wu S., Pyrc J.J., Ross A.H., RA Dietzschold B., Speicher D., Koprowski H.; RT "Sequence investigation of the major gastrointestinal tumor-associated RT antigen gene family, GA733."; RL Proc. Natl. Acad. Sci. U.S.A. 86:27-31(1989). RN [11] RP PROTEIN SEQUENCE OF 82-100, AND SUBUNIT. RX PubMed=7693697; DOI=10.1016/s0021-9258(20)80515-8; RA Bjoerk P., Joensson U., Svedberg H., Larsson K., Lind P., Dillner J., RA Hedlund G., Dohlsten M., Kalland T.; RT "Isolation, partial characterization, and molecular cloning of a human RT colon adenocarcinoma cell-surface glycoprotein recognized by the C215 mouse RT monoclonal antibody."; RL J. Biol. Chem. 268:24232-24241(1993). RN [12] RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-74 AND ASN-111. RX PubMed=11080501; DOI=10.1074/jbc.m008839200; RA Chong J.M., Speicher D.W.; RT "Determination of disulfide bond assignments and N-glycosylation sites of RT the human gastrointestinal carcinoma antigen GA733-2 (CO17-1A, EGP, KS1-4, RT KSA, and Ep-CAM)."; RL J. Biol. Chem. 276:5804-5813(2001). RN [13] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15195135; DOI=10.1038/sj.onc.1207610; RA Muenz M., Kieu C., Mack B., Schmitt B., Zeidler R., Gires O.; RT "The carcinoma-associated antigen EpCAM upregulates c-myc and induces cell RT proliferation."; RL Oncogene 23:5748-5758(2004). RN [14] RP FUNCTION. RX PubMed=15922867; DOI=10.1016/j.canlet.2004.11.048; RA Muenz M., Zeidler R., Gires O.; RT "The tumour-associated antigen EpCAM upregulates the fatty acid binding RT protein E-FABP."; RL Cancer Lett. 225:151-157(2005). RN [15] RP SUBCELLULAR LOCATION, AND INTERACTION WITH CLDN7. RX PubMed=16054130; DOI=10.1016/j.yexcr.2005.06.013; RA Ladwein M., Pape U.F., Schmidt D.S., Schnoelzer M., Fiedler S., RA Langbein L., Franke W.W., Moldenhauer G., Zoeller M.; RT "The cell-cell adhesion molecule EpCAM interacts directly with the tight RT junction protein claudin-7."; RL Exp. Cell Res. 309:345-357(2005). RN [16] RP GLYCOSYLATION AT ASN-74; ASN-111 AND ASN-198, AND MUTAGENESIS OF ASN-74; RP ASN-111 AND ASN-198. RX PubMed=18508581; DOI=10.2741/3075; RA Munz M., Fellinger K., Hofmann T., Schmitt B., Gires O.; RT "Glycosylation is crucial for stability of tumour and cancer stem cell RT antigen EpCAM."; RL Front. Biosci. 13:5195-5201(2008). RN [17] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-198. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [18] RP INVOLVEMENT IN LYNCH8. RX PubMed=19098912; DOI=10.1038/ng.283; RA Ligtenberg M.J., Kuiper R.P., Chan T.L., Goossens M., Hebeda K.M., RA Voorendt M., Lee T.Y., Bodmer D., Hoenselaar E., Hendriks-Cornelissen S.J., RA Tsui W.Y., Kong C.K., Brunner H.G., van Kessel A.G., Yuen S.T., RA van Krieken J.H., Leung S.Y., Hoogerbrugge N.; RT "Heritable somatic methylation and inactivation of MSH2 in families with RT Lynch syndrome due to deletion of the 3' exons of TACSTD1."; RL Nat. Genet. 41:112-117(2009). RN [19] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=20064925; DOI=10.1074/jbc.m109.077081; RA Lu T.Y., Lu R.M., Liao M.Y., Yu J., Chung C.H., Kao C.F., Wu H.C.; RT "Epithelial cell adhesion molecule regulation is associated with the RT maintenance of the undifferentiated phenotype of human embryonic stem RT cells."; RL J. Biol. Chem. 285:8719-8732(2010). RN [20] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=19785009; DOI=10.1002/stem.221; RA Ng V.Y., Ang S.N., Chan J.X., Choo A.B.; RT "Characterization of epithelial cell adhesion molecule as a surface marker RT on undifferentiated human embryonic stem cells."; RL Stem Cells 28:29-35(2010). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [22] RP VARIANT DIAR5 TYR-66. RX PubMed=18572020; DOI=10.1053/j.gastro.2008.05.036; RA Sivagnanam M., Mueller J.L., Lee H., Chen Z., Nelson S.F., Turner D., RA Zlotkin S.H., Pencharz P.B., Ngan B.Y., Libiger O., Schork N.J., RA Lavine J.E., Taylor S., Newbury R.O., Kolodner R.D., Hoffman H.M.; RT "Identification of EpCAM as the gene for congenital tufting enteropathy."; RL Gastroenterology 135:429-437(2008). CC -!- FUNCTION: May act as a physical homophilic interaction molecule between CC intestinal epithelial cells (IECs) and intraepithelial lymphocytes CC (IELs) at the mucosal epithelium for providing immunological barrier as CC a first line of defense against mucosal infection. Plays a role in CC embryonic stem cells proliferation and differentiation. Up-regulates CC the expression of FABP5, MYC and cyclins A and E. CC {ECO:0000269|PubMed:15195135, ECO:0000269|PubMed:15922867, CC ECO:0000269|PubMed:19785009, ECO:0000269|PubMed:20064925}. CC -!- SUBUNIT: Monomer. Interacts with phosphorylated CLDN7. CC {ECO:0000269|PubMed:16054130, ECO:0000269|PubMed:7693697}. CC -!- INTERACTION: CC P16422; P27797: CALR; NbExp=3; IntAct=EBI-1171184, EBI-1049597; CC P16422; P12830: CDH1; NbExp=3; IntAct=EBI-1171184, EBI-727477; CC P16422; Q15078: CDK5R1; NbExp=3; IntAct=EBI-1171184, EBI-746189; CC P16422; P36957: DLST; NbExp=3; IntAct=EBI-1171184, EBI-351007; CC P16422; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-1171184, EBI-1055945; CC -!- SUBCELLULAR LOCATION: Lateral cell membrane CC {ECO:0000269|PubMed:15195135, ECO:0000269|PubMed:16054130, CC ECO:0000269|PubMed:19785009}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:16054130}. Cell junction, tight junction CC {ECO:0000269|PubMed:16054130}. Note=Colocalizes with CLDN7 at the CC lateral cell membrane and tight junction. CC {ECO:0000269|PubMed:16054130}. CC -!- TISSUE SPECIFICITY: Highly and selectively expressed by CC undifferentiated rather than differentiated embryonic stem cells (ESC). CC Levels rapidly diminish as soon as ESC's differentiate (at protein CC levels). Expressed in almost all epithelial cell membranes but not on CC mesodermal or neural cell membranes. Found on the surface of CC adenocarcinoma. {ECO:0000269|PubMed:20064925}. CC -!- PTM: Hyperglycosylated in carcinoma tissue as compared with autologous CC normal epithelia. Glycosylation at Asn-198 is crucial for protein CC stability. {ECO:0000269|PubMed:11080501, ECO:0000269|PubMed:18508581, CC ECO:0000269|PubMed:19159218}. CC -!- DISEASE: Diarrhea 5, with tufting enteropathy, congenital (DIAR5) CC [MIM:613217]: An intractable diarrhea of infancy characterized by CC villous atrophy and absence of inflammation, with intestinal epithelial CC cell dysplasia manifesting as focal epithelial tufts in the duodenum CC and jejunum. {ECO:0000269|PubMed:18572020}. Note=The disease is caused CC by variants affecting the gene represented in this entry. CC -!- DISEASE: Lynch syndrome 8 (LYNCH8) [MIM:613244]: A form of Lynch CC syndrome, an autosomal dominant disease associated with marked increase CC in cancer susceptibility. It is characterized by a familial CC predisposition to early-onset colorectal carcinoma (CRC) and extra- CC colonic tumors of the gastrointestinal, urological and female CC reproductive tracts. Lynch syndrome is reported to be the most common CC form of inherited colorectal cancer in the Western world. Clinically, CC it is often divided into two subgroups. Type I is characterized by CC hereditary predisposition to colorectal cancer, a young age of onset, CC and carcinoma observed in the proximal colon. Type II is characterized CC by increased risk for cancers in certain tissues such as the uterus, CC ovary, breast, stomach, small intestine, skin, and larynx in addition CC to the colon. Diagnosis of classical Lynch syndrome is based on the CC Amsterdam criteria: 3 or more relatives affected by colorectal cancer, CC one a first degree relative of the other two; 2 or more generation CC affected; 1 or more colorectal cancers presenting before 50 years of CC age; exclusion of hereditary polyposis syndromes. The term 'suspected CC Lynch syndrome' or 'incomplete Lynch syndrome' can be used to describe CC families who do not or only partially fulfill the Amsterdam criteria, CC but in whom a genetic basis for colon cancer is strongly suspected. CC {ECO:0000269|PubMed:19098912}. Note=The disease is caused by variants CC affecting the gene represented in this entry. LYNCH8 results from CC heterozygous deletion of 3-prime exons of EPCAM and intergenic regions CC directly upstream of MSH2, resulting in transcriptional read-through CC and epigenetic silencing of MSH2 in tissues expressing EPCAM. CC -!- SIMILARITY: Belongs to the EPCAM family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42459/TACSTD1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M32325; AAA36151.1; -; mRNA. DR EMBL; X14758; CAA32870.1; -; mRNA. DR EMBL; M26481; AAA59543.1; -; mRNA. DR EMBL; M32306; AAA35723.1; -; mRNA. DR EMBL; M33011; AAA35861.1; -; mRNA. DR EMBL; M93036; AAB00775.1; -; Genomic_DNA. DR EMBL; M93029; AAB00775.1; JOINED; Genomic_DNA. DR EMBL; M93030; AAB00775.1; JOINED; Genomic_DNA. DR EMBL; M93031; AAB00775.1; JOINED; Genomic_DNA. DR EMBL; M93032; AAB00775.1; JOINED; Genomic_DNA. DR EMBL; M93033; AAB00775.1; JOINED; Genomic_DNA. DR EMBL; M93034; AAB00775.1; JOINED; Genomic_DNA. DR EMBL; M93035; AAB00775.1; JOINED; Genomic_DNA. DR EMBL; CR542259; CAG47055.1; -; mRNA. DR EMBL; CR542283; CAG47078.1; -; mRNA. DR EMBL; AC079775; AAY15095.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00218.1; -; Genomic_DNA. DR EMBL; BC014785; AAH14785.1; -; mRNA. DR CCDS; CCDS1833.1; -. DR PIR; B48149; B48149. DR RefSeq; NP_002345.2; NM_002354.2. DR PDB; 4MZV; X-ray; 1.86 A; A=24-265. DR PDB; 6I07; X-ray; 2.35 A; C/D=24-265. DR PDBsum; 4MZV; -. DR PDBsum; 6I07; -. DR AlphaFoldDB; P16422; -. DR SMR; P16422; -. DR BioGRID; 110250; 25. DR CORUM; P16422; -. DR IntAct; P16422; 16. DR MINT; P16422; -. DR STRING; 9606.ENSP00000263735; -. DR ChEMBL; CHEMBL3580493; -. DR DrugBank; DB06607; Catumaxomab. DR DrugBank; DB11075; Hypromellose. DR DrugBank; DB05831; ING-1. DR DrugBank; DB05319; Oportuzumab monatox. DR DrugBank; DB09336; Technetium Tc-99m nofetumomab merpentan. DR GlyConnect; 1217; 34 N-Linked glycans (3 sites). DR GlyCosmos; P16422; 3 sites, 34 glycans. DR GlyGen; P16422; 6 sites, 34 N-linked glycans (3 sites), 2 O-linked glycans (3 sites). DR iPTMnet; P16422; -. DR MetOSite; P16422; -. DR PhosphoSitePlus; P16422; -. DR SwissPalm; P16422; -. DR BioMuta; EPCAM; -. DR DMDM; 160266056; -. DR CPTAC; CPTAC-502; -. DR CPTAC; CPTAC-503; -. DR EPD; P16422; -. DR jPOST; P16422; -. DR MassIVE; P16422; -. DR MaxQB; P16422; -. DR PaxDb; 9606-ENSP00000263735; -. DR PeptideAtlas; P16422; -. DR ProteomicsDB; 53359; -. DR Pumba; P16422; -. DR ABCD; P16422; 17 sequenced antibodies. DR Antibodypedia; 3539; 5262 antibodies from 61 providers. DR DNASU; 4072; -. DR Ensembl; ENST00000263735.9; ENSP00000263735.4; ENSG00000119888.11. DR GeneID; 4072; -. DR KEGG; hsa:4072; -. DR MANE-Select; ENST00000263735.9; ENSP00000263735.4; NM_002354.3; NP_002345.2. DR UCSC; uc002rvx.4; human. DR AGR; HGNC:11529; -. DR CTD; 4072; -. DR DisGeNET; 4072; -. DR GeneCards; EPCAM; -. DR GeneReviews; EPCAM; -. DR HGNC; HGNC:11529; EPCAM. DR HPA; ENSG00000119888; Tissue enhanced (intestine). DR MalaCards; EPCAM; -. DR MIM; 185535; gene. DR MIM; 613217; phenotype. DR MIM; 613244; phenotype. DR neXtProt; NX_P16422; -. DR OpenTargets; ENSG00000119888; -. DR Orphanet; 92050; Congenital tufting enteropathy. DR Orphanet; 144; Lynch syndrome. DR PharmGKB; PA35493; -. DR VEuPathDB; HostDB:ENSG00000119888; -. DR eggNOG; ENOG502QVSU; Eukaryota. DR GeneTree; ENSGT00390000018245; -. DR HOGENOM; CLU_075326_0_0_1; -. DR InParanoid; P16422; -. DR OMA; TQNSVIC; -. DR OrthoDB; 5305981at2759; -. DR PhylomeDB; P16422; -. DR TreeFam; TF332767; -. DR BRENDA; 2.4.1.37; 2681. DR BRENDA; 2.4.1.40; 2681. DR PathwayCommons; P16422; -. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR SignaLink; P16422; -. DR SIGNOR; P16422; -. DR BioGRID-ORCS; 4072; 34 hits in 1164 CRISPR screens. DR ChiTaRS; EPCAM; human. DR GeneWiki; Epithelial_cell_adhesion_molecule; -. DR GenomeRNAi; 4072; -. DR Pharos; P16422; Tbio. DR PRO; PR:P16422; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P16422; Protein. DR Bgee; ENSG00000119888; Expressed in jejunal mucosa and 176 other cell types or tissues. DR ExpressionAtlas; P16422; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI. DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IBA:GO_Central. DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB. DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; IDA:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB. DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IMP:UniProtKB. DR GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB. DR GO; GO:0001657; P:ureteric bud development; IEA:Ensembl. DR CDD; cd00191; TY; 1. DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 1. DR InterPro; IPR049420; EPCAM-Trop-2_C. DR InterPro; IPR043406; EPCAM/Trop-2. DR InterPro; IPR041630; EpCAM_N. DR InterPro; IPR000716; Thyroglobulin_1. DR InterPro; IPR036857; Thyroglobulin_1_sf. DR PANTHER; PTHR14168:SF2; EPITHELIAL CELL ADHESION MOLECULE; 1. DR PANTHER; PTHR14168; TUMOR-ASSOCIATED CALCIUM SIGNAL TRANSDUCER; 1. DR Pfam; PF21283; EPCAM-Trop-2_C; 1. DR Pfam; PF18635; EpCAM_N; 1. DR Pfam; PF00086; Thyroglobulin_1; 1. DR SMART; SM00211; TY; 1. DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1. DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1. DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1. DR Genevisible; P16422; HS. PE 1: Evidence at protein level; KW 3D-structure; Cell junction; Cell membrane; Direct protein sequencing; KW Disease variant; Disulfide bond; Glycoprotein; KW Hereditary nonpolyposis colorectal cancer; Membrane; Reference proteome; KW Repeat; Signal; Tight junction; Transmembrane; Transmembrane helix; KW Tumor antigen. FT SIGNAL 1..23 FT /evidence="ECO:0000255" FT CHAIN 24..314 FT /note="Epithelial cell adhesion molecule" FT /id="PRO_0000022467" FT TOPO_DOM 24..265 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 266..288 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 289..314 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 63..135 FT /note="Thyroglobulin type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500" FT CARBOHYD 74 FT /note="N-linked (GlcNAc...) asparagine; partial" FT /evidence="ECO:0000269|PubMed:11080501, FT ECO:0000269|PubMed:18508581" FT CARBOHYD 111 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11080501, FT ECO:0000269|PubMed:18508581" FT CARBOHYD 198 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18508581, FT ECO:0000269|PubMed:19159218" FT DISULFID 27..46 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500, FT ECO:0000269|PubMed:11080501" FT DISULFID 29..59 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500, FT ECO:0000269|PubMed:11080501" FT DISULFID 38..48 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500, FT ECO:0000269|PubMed:11080501" FT DISULFID 66..99 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500, FT ECO:0000269|PubMed:11080501" FT DISULFID 110..116 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500, FT ECO:0000269|PubMed:11080501" FT DISULFID 118..135 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500, FT ECO:0000269|PubMed:11080501" FT VARIANT 66 FT /note="C -> Y (in DIAR5; dbSNP:rs267606785)" FT /evidence="ECO:0000269|PubMed:18572020" FT /id="VAR_063829" FT VARIANT 115 FT /note="M -> T (in dbSNP:rs1126497)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:2108441, ECO:0000269|PubMed:2463074, FT ECO:0000269|PubMed:2469722" FT /id="VAR_018329" FT MUTAGEN 74 FT /note="N->A: Changed glycosylation pattern. Complete loss FT of glycosylation and substantial decrease in protein FT expression; when associated with A-111 and A-198." FT /evidence="ECO:0000269|PubMed:18508581" FT MUTAGEN 111 FT /note="N->A: Changed glycosylation pattern. Complete loss FT of glycosylation and substantial decrease in protein FT expression; when associated with A-74 and A-198." FT /evidence="ECO:0000269|PubMed:18508581" FT MUTAGEN 198 FT /note="N->A: Decreased glycosylation, reduced protein FT stability and significant decrease in protein expression. FT Complete loss of glycosylation and substantial decrease in FT protein expression; when associated with A-74 and A-111." FT /evidence="ECO:0000269|PubMed:18508581" FT CONFLICT 277 FT /note="I -> M (in Ref. 1; AAA36151/CAA32870 and 2; FT AAA59543)" FT /evidence="ECO:0000305" FT CONFLICT 303 FT /note="K -> R (in Ref. 6; CAG47055)" FT /evidence="ECO:0000305" FT STRAND 35..40 FT /evidence="ECO:0007829|PDB:4MZV" FT STRAND 46..50 FT /evidence="ECO:0007829|PDB:4MZV" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:4MZV" FT HELIX 65..72 FT /evidence="ECO:0007829|PDB:4MZV" FT TURN 73..75 FT /evidence="ECO:0007829|PDB:4MZV" FT STRAND 107..111 FT /evidence="ECO:0007829|PDB:4MZV" FT TURN 112..114 FT /evidence="ECO:0007829|PDB:4MZV" FT STRAND 115..120 FT /evidence="ECO:0007829|PDB:4MZV" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:4MZV" FT STRAND 141..150 FT /evidence="ECO:0007829|PDB:4MZV" FT HELIX 159..173 FT /evidence="ECO:0007829|PDB:4MZV" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:4MZV" FT STRAND 181..187 FT /evidence="ECO:0007829|PDB:4MZV" FT STRAND 190..196 FT /evidence="ECO:0007829|PDB:4MZV" FT TURN 199..201 FT /evidence="ECO:0007829|PDB:4MZV" FT HELIX 209..220 FT /evidence="ECO:0007829|PDB:4MZV" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:4MZV" FT STRAND 234..237 FT /evidence="ECO:0007829|PDB:6I07" FT HELIX 244..246 FT /evidence="ECO:0007829|PDB:4MZV" FT STRAND 248..255 FT /evidence="ECO:0007829|PDB:4MZV" SQ SEQUENCE 314 AA; 34932 MW; 023FCE418B2F1079 CRC64; MAPPQVLAFG LLLAAATATF AAAQEECVCE NYKLAVNCFV NNNRQCQCTS VGAQNTVICS KLAAKCLVMK AEMNGSKLGR RAKPEGALQN NDGLYDPDCD ESGLFKAKQC NGTSMCWCVN TAGVRRTDKD TEITCSERVR TYWIIIELKH KAREKPYDSK SLRTALQKEI TTRYQLDPKF ITSILYENNV ITIDLVQNSS QKTQNDVDIA DVAYYFEKDV KGESLFHSKK MDLTVNGEQL DLDPGQTLIY YVDEKAPEFS MQGLKAGVIA VIVVVVIAVV AGIVVLVISR KKRMAKYEKA EIKEMGEMHR ELNA //